CAZyme Information: MGYG000002614_01047

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola
• CAZyme ID: MGYG000002614_01047
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
342		38182.38	5.6367

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002614	2560607	MAG	China	Asia

• Gene Location: Start: 10817; End: 11845 Strand: -

Full Sequence      

MKNTYGILLFLWACICVSCGTSGRQQPDTSKDIVLAYVTSNGKTLPDPSLVTHINYAFGH
VDSTFSKVVIDRESRLQEIANLKKDAPHLKVLLSIGGWGSGHFSEMAADEQCRLSFARDC
RRVVDQFGLDGIDIDWEYPTSRAAGISASDADTENYTLLMRDIREAIGTGKLLTLASAAN
AKYIDFKAIDPYIDFVNIMTYDMNRPPYHHSALYRSPRVDRRSCEESVEAHLQQGIPASK
LVLGAPFYGHAAPPMSDFIDYRDIVKLEGYEACWDTLACVPYLADKEGCLICTYENPRSL
AAKCAFVRQKGLLGMMYWEYNTDDEAGSLRKAVYEGMRGDKQ

Enzyme Prediction     

No EC number prediction in MGYG000002614_01047.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	47	328	1.4e-69	0.8581081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.60e-102	34	323	1	322	The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.
smart00636	Glyco_18	6.74e-87	34	323	2	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	1.74e-80	34	323	2	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	4.35e-69	34	327	1	345	This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
COG3325	ChiA	6.96e-62	47	336	61	435	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRO23424.1	1.04e-166	1	338	1	335
QIK61506.1	2.61e-134	33	334	41	342
ATP56025.1	3.01e-134	1	337	1	339
QIK56154.1	5.25e-134	16	334	18	342
ADV45176.1	3.33e-133	7	341	6	343

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6HM1_A	9.81e-55	47	342	27	400	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	1.05e-54	47	342	30	403	CrystalStructure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine, a hydrolyzed product of hexasaccharide at 1.7 Angstrom resolution [Serratia proteamaculans 568]
4LGX_A	1.13e-54	47	342	33	406	Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
6F8N_A	3.77e-54	47	342	35	408	Keyresidues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [Serratia proteamaculans 568],6F8N_B Key residues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [Serratia proteamaculans 568]
4NZC_A	5.11e-54	47	324	30	384	Crystalstructure of Chitinase D from Serratia proteamaculans at 1.45 Angstrom resolution [Serratia proteamaculans 568],4Q22_A Crystal structure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine at 1.93 Angstrom resolution [Serratia proteamaculans 568]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9W092	1.24e-38	47	338	66	406	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
P20533	3.66e-38	10	323	75	438	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9D7Q1	8.59e-35	47	329	47	367	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
Q13231	1.18e-33	47	327	47	367	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q95M17	3.31e-28	47	329	47	371	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000002	1.000044	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002614_01047.